Related Experiment Video

Updated: Jun 18, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
11:19

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the

Yinhua Yang1, Amanda Nga-Sze Mak, Pang-Chui Shaw

  • 1Chemistry Department and Open Laboratory of Chemical Biology, Institute of Molecular Technology for Drug Discovery and Synthesis, The University of Hong Kong, Pokfulam Road, Hong Kong, PR China.

Journal of Molecular Biology
|November 11, 2009
PubMed

Insights

This study reveals the unique structure of a maize ribosome-inactivating protein (RIP) mutant. Its distinct features, including a relocated P2 binding site, offer insights into the molecular mechanisms of this protein synthesis inhibitor.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Ribosome-inactivating proteins (RIPs) are N-glycosidases that inhibit protein synthesis by depurinating ribosomal RNA.
  • Maize RIP, a type III RIP, is synthesized as an inactive precursor requiring removal of an internal region for activation.

Purpose of the Study:

  • To determine the first solution structure of a type III RIP, specifically a 28-kDa active mutant of maize RIP (MOD).
  • To investigate structural differences and identify the ribosomal protein P2 binding site in MOD.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the solution structure of MOD.
  • NMR chemical shift perturbation experiments to map the P2 binding site.

Main Results:

  • The overall structure of MOD is similar to other RIPs, but with notable differences in beta6, alphaB segments, and the C-terminal domain.
  • An alpha-helix replaces an antiparallel beta-sheet in the C-terminal domain of MOD.
  • The P2 binding site was identified in the N-terminal domain of MOD, near the internal inactivation region.

Conclusions:

  • The unique structural features of MOD, including the relocated P2 binding site, provide crucial insights into the molecular mechanism of this distinct type of RIP.
  • These findings contribute to understanding RIP function and potential applications.

More Related Videos

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling06:58

Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling

Published on: October 7, 2021

Related Concept Videos

Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...